FMO DATABASE

FMODB ID: 8JZQY

Calculation Name: 1JPE-A-Xray309

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JPE

Chain ID: A

ChEMBL ID:

UniProt ID: P36655

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	117
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-946006.34301
FMO2-HF: Nuclear repulsion	899940.94205
FMO2-HF: Total energy	-46065.40096
FMO2-MP2: Total energy	-46201.727365

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:9:ACE )

Summations of interaction energy for fragment #1(A:9:ACE )

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
1.679	2.631	-0.006	-0.439	-0.507	-0.001

Interaction energy analysis for fragmet #1(A:9:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.004

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

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Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	11	PHE	0	-0.005	0.020	3.841	0.922	1.847	-0.006	-0.436	-0.483	-0.001
4	A	12	VAL	0	-0.020	0.004	5.950	0.157	0.157	0.000	0.000	0.000	0.000
5	A	13	PRO	0	0.070	0.046	8.811	0.133	0.133	0.000	0.000	0.000	0.000
6	A	14	ALA	0	0.103	0.043	12.188	-0.040	-0.040	0.000	0.000	0.000	0.000
7	A	15	ASP	-1	-0.824	-0.893	14.079	-0.174	-0.174	0.000	0.000	0.000	0.000
8	A	16	GLN	0	-0.070	-0.040	12.522	0.043	0.043	0.000	0.000	0.000	0.000
9	A	17	ALA	0	-0.039	-0.006	11.676	-0.026	-0.026	0.000	0.000	0.000	0.000
10	A	18	PHE	0	-0.020	-0.004	13.565	0.027	0.027	0.000	0.000	0.000	0.000
11	A	19	ALA	0	0.028	0.016	17.161	0.020	0.020	0.000	0.000	0.000	0.000
12	A	20	PHE	0	-0.034	-0.016	19.707	0.015	0.015	0.000	0.000	0.000	0.000
13	A	21	ASP	-1	-0.884	-0.940	22.960	-0.111	-0.111	0.000	0.000	0.000	0.000
14	A	22	PHE	0	-0.043	-0.022	26.416	0.005	0.005	0.000	0.000	0.000	0.000
15	A	23	GLN	0	0.030	0.017	30.042	0.002	0.002	0.000	0.000	0.000	0.000
16	A	24	GLN	0	-0.003	-0.003	33.351	0.000	0.000	0.000	0.000	0.000	0.000
17	A	25	ASN	0	-0.032	-0.010	36.739	0.003	0.003	0.000	0.000	0.000	0.000
18	A	26	GLN	0	0.014	-0.001	40.117	0.004	0.004	0.000	0.000	0.000	0.000
19	A	27	HIS	1	0.911	0.934	41.189	0.035	0.035	0.000	0.000	0.000	0.000
20	A	28	ASP	-1	-0.912	-0.917	38.770	-0.047	-0.047	0.000	0.000	0.000	0.000
21	A	29	LEU	0	0.018	0.008	33.384	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	30	ASN	0	-0.031	-0.014	30.813	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	31	LEU	0	0.001	0.003	28.230	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	32	THR	0	0.002	-0.006	24.787	0.000	0.000	0.000	0.000	0.000	0.000
25	A	33	TRP	0	0.007	0.001	20.796	0.000	0.000	0.000	0.000	0.000	0.000
26	A	34	GLN	0	-0.057	-0.041	20.031	0.000	0.000	0.000	0.000	0.000	0.000
27	A	35	ILE	0	-0.046	-0.022	16.026	-0.016	-0.016	0.000	0.000	0.000	0.000
28	A	36	LYS	1	0.912	0.978	10.356	0.798	0.798	0.000	0.000	0.000	0.000
29	A	37	ASP	-1	-0.872	-0.947	13.727	-0.362	-0.362	0.000	0.000	0.000	0.000
30	A	38	GLY	0	0.016	0.012	10.729	-0.117	-0.117	0.000	0.000	0.000	0.000
31	A	39	TYR	0	-0.070	-0.045	7.395	-0.095	-0.095	0.000	0.000	0.000	0.000
32	A	40	TYR	0	-0.027	-0.019	12.779	0.029	0.029	0.000	0.000	0.000	0.000
33	A	41	LEU	0	-0.014	0.000	16.099	0.007	0.007	0.000	0.000	0.000	0.000
34	A	42	TYR	0	0.018	-0.022	17.332	0.005	0.005	0.000	0.000	0.000	0.000
35	A	43	ARG	1	0.872	0.940	21.014	0.053	0.053	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.915	0.929	24.594	0.033	0.033	0.000	0.000	0.000	0.000
37	A	45	GLN	0	0.000	0.017	21.269	0.006	0.006	0.000	0.000	0.000	0.000
38	A	46	ILE	0	-0.026	-0.002	23.952	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	47	ARG	1	0.822	0.909	25.924	0.046	0.046	0.000	0.000	0.000	0.000
40	A	48	ILE	0	0.004	-0.007	28.797	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	49	THR	0	-0.025	-0.005	31.372	0.003	0.003	0.000	0.000	0.000	0.000
42	A	50	PRO	0	0.002	0.025	34.134	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	51	GLU	-1	-0.798	-0.900	34.966	-0.034	-0.034	0.000	0.000	0.000	0.000
44	A	52	HIS	0	-0.015	-0.013	38.617	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	53	ALA	0	0.074	0.022	39.740	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	54	LYS	1	0.891	0.953	41.486	0.024	0.024	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.021	0.002	36.224	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	56	ALA	0	-0.037	-0.011	40.190	0.002	0.002	0.000	0.000	0.000	0.000
49	A	57	ASP	-1	-0.905	-0.947	38.600	-0.031	-0.031	0.000	0.000	0.000	0.000
50	A	58	VAL	0	-0.005	-0.009	32.377	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	59	GLN	0	-0.038	-0.015	34.270	0.001	0.001	0.000	0.000	0.000	0.000
52	A	60	LEU	0	-0.026	-0.011	28.025	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	61	PRO	0	0.035	0.019	27.832	0.004	0.004	0.000	0.000	0.000	0.000
54	A	62	GLN	0	-0.047	-0.023	28.308	0.004	0.004	0.000	0.000	0.000	0.000
55	A	63	GLY	0	0.010	0.000	25.226	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	64	VAL	0	-0.011	0.002	21.599	0.007	0.007	0.000	0.000	0.000	0.000
57	A	65	TRP	0	-0.033	-0.022	23.266	0.002	0.002	0.000	0.000	0.000	0.000
58	A	66	HIS	0	0.015	0.002	15.285	-0.018	-0.018	0.000	0.000	0.000	0.000
59	A	67	GLU	-1	-0.965	-0.988	19.210	0.019	0.019	0.000	0.000	0.000	0.000
60	A	68	ASP	-1	-0.777	-0.859	15.582	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	69	GLU	-1	-0.871	-0.954	14.591	0.085	0.085	0.000	0.000	0.000	0.000
62	A	70	PHE	0	-0.085	-0.025	12.588	0.006	0.006	0.000	0.000	0.000	0.000
63	A	71	TYR	0	-0.068	-0.042	18.265	0.000	0.000	0.000	0.000	0.000	0.000
64	A	72	GLY	0	0.028	0.032	20.395	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	73	LYS	1	0.935	0.978	21.112	0.007	0.007	0.000	0.000	0.000	0.000
66	A	74	SER	0	-0.008	-0.016	21.332	0.001	0.001	0.000	0.000	0.000	0.000
67	A	75	GLU	-1	-0.825	-0.884	22.724	-0.057	-0.057	0.000	0.000	0.000	0.000
68	A	76	ILE	0	-0.009	-0.017	18.039	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	77	TYR	0	-0.058	-0.062	20.492	0.005	0.005	0.000	0.000	0.000	0.000
70	A	78	ARG	1	0.889	0.899	14.071	0.181	0.181	0.000	0.000	0.000	0.000
71	A	79	ASP	-1	-0.859	-0.909	18.173	-0.177	-0.177	0.000	0.000	0.000	0.000
72	A	80	ARG	1	0.907	0.930	19.807	0.136	0.136	0.000	0.000	0.000	0.000
73	A	81	LEU	0	-0.034	0.021	22.331	0.012	0.012	0.000	0.000	0.000	0.000
74	A	82	THR	0	-0.010	-0.018	24.549	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	83	LEU	0	-0.016	-0.015	28.094	0.006	0.006	0.000	0.000	0.000	0.000
76	A	84	PRO	0	-0.010	0.008	30.303	0.000	0.000	0.000	0.000	0.000	0.000
77	A	85	VAL	0	0.012	-0.006	32.947	0.003	0.003	0.000	0.000	0.000	0.000
78	A	86	THR	0	0.037	0.023	35.697	0.000	0.000	0.000	0.000	0.000	0.000
79	A	87	ILE	0	0.029	0.015	37.581	0.002	0.002	0.000	0.000	0.000	0.000
80	A	88	ASN	0	0.003	-0.001	40.865	0.000	0.000	0.000	0.000	0.000	0.000
81	A	89	GLN	0	-0.024	-0.034	43.575	0.002	0.002	0.000	0.000	0.000	0.000
82	A	90	ALA	0	0.032	0.029	41.557	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	91	SER	0	-0.001	0.015	43.343	0.001	0.001	0.000	0.000	0.000	0.000
84	A	92	ALA	0	0.053	0.012	43.065	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	93	GLY	0	-0.011	-0.004	40.319	0.001	0.001	0.000	0.000	0.000	0.000
86	A	94	ALA	0	-0.025	0.008	39.418	0.000	0.000	0.000	0.000	0.000	0.000
87	A	95	THR	0	-0.015	-0.013	34.324	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	96	LEU	0	-0.002	0.008	32.493	0.003	0.003	0.000	0.000	0.000	0.000
89	A	97	THR	0	0.012	0.006	29.399	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	98	VAL	0	0.000	-0.010	26.081	0.003	0.003	0.000	0.000	0.000	0.000
91	A	99	THR	0	-0.021	-0.002	24.224	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	100	TYR	0	0.047	0.032	19.294	0.006	0.006	0.000	0.000	0.000	0.000
93	A	101	GLN	0	0.042	0.003	17.473	0.003	0.003	0.000	0.000	0.000	0.000
94	A	102	GLY	0	0.048	0.017	16.160	0.002	0.002	0.000	0.000	0.000	0.000
95	A	109	CYS	0	-0.067	0.004	9.819	-0.077	-0.077	0.000	0.000	0.000	0.000
96	A	104	ALA	0	0.049	0.009	7.957	-0.070	-0.070	0.000	0.000	0.000	0.000
97	A	105	ASP	-1	-0.737	-0.857	9.886	-0.153	-0.153	0.000	0.000	0.000	0.000
98	A	106	ALA	0	-0.088	-0.041	4.675	0.025	0.052	0.000	-0.003	-0.024	0.000
99	A	107	GLY	0	0.013	0.023	6.812	0.247	0.247	0.000	0.000	0.000	0.000
100	A	108	PHE	0	-0.034	-0.023	5.447	0.102	0.102	0.000	0.000	0.000	0.000
101	A	110	TYR	0	-0.048	-0.048	9.838	0.014	0.014	0.000	0.000	0.000	0.000
102	A	111	PRO	0	-0.006	0.000	13.922	0.015	0.015	0.000	0.000	0.000	0.000
103	A	112	PRO	0	0.010	-0.010	17.370	-0.021	-0.021	0.000	0.000	0.000	0.000
104	A	113	GLH	0	-0.053	-0.030	18.256	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	114	THR	0	-0.015	-0.040	21.122	0.003	0.003	0.000	0.000	0.000	0.000
106	A	115	LYS	1	0.832	0.921	20.974	0.127	0.127	0.000	0.000	0.000	0.000
107	A	116	THR	0	0.020	0.006	26.164	0.004	0.004	0.000	0.000	0.000	0.000
108	A	117	VAL	0	-0.016	-0.007	29.669	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	118	PRO	0	-0.017	0.001	31.640	0.005	0.005	0.000	0.000	0.000	0.000
110	A	119	LEU	0	-0.022	-0.012	34.929	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	120	SER	0	-0.039	-0.025	37.560	0.002	0.002	0.000	0.000	0.000	0.000
112	A	121	GLU	-1	-0.938	-0.980	40.438	-0.029	-0.029	0.000	0.000	0.000	0.000
113	A	122	VAL	0	-0.057	-0.024	42.560	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	123	VAL	0	0.019	0.003	45.357	0.001	0.001	0.000	0.000	0.000	0.000
115	A	124	ALA	0	-0.034	-0.033	48.204	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	125	ASN	0	-0.015	-0.005	49.124	0.001	0.001	0.000	0.000	0.000	0.000
117	A	126	NME	0	0.016	0.027	48.123	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ACE )